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Author Details

Dmitry M Korzhnev
University of Connecticut Health Center
1995
75
32
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
36711877Activation Dynamics of Ubiquitin Specific Protease 7.bioRxiv2023
37473756Conformational exchange at a C<sub>2</sub>H<sub>2</sub> zinc-binding site facilitates redox sensing by the PML protein.Structure2023
37129702Backbone and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes.Biomol NMR Assign2023
36592930Evolution of Rev7 interactions in eukaryotic TLS DNA polymerase Polζ.J Biol Chem2023
35192840Architecture of the two metal-binding sites in prolactin.Biophys J2022
35608245DNA Sequence Specificity Reveals a Role of the HLTF HIRAN Domain in the Recognition of Trinucleotide Repeats.Biochemistry2022
35536398Backbone and ILV side-chain NMR resonance assignments of the catalytic domain of human deubiquitinating enzyme USP7.Biomol NMR Assign2022
35687262ILV methyl NMR resonance assignments of the 81 kDa E. coli β-clamp.Biomol NMR Assign2022
33314657Structure-Based Drug Design of Phenazopyridine Derivatives as Inhibitors of Rev1 Interactions in Translesion Synthesis.ChemMedChem2021
33761093NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex γ subunit.Biomol NMR Assign2021
34458830Targeting protein-protein interactions in the DNA damage response pathways for cancer chemotherapy.RSC Chem Biol2021
34771454REV1 Inhibition Enhances Radioresistance and Autophagy.Cancers (Basel)2021
31361935Virtual Pharmacophore Screening Identifies Small-Molecule Inhibitors of the Rev1-CT/RIR Protein-Protein Interaction.ChemMedChem2019
31627876The Rev1-Polζ translesion synthesis mutasome: Structure, interactions and inhibition.Enzymes2019
30289707Structural Approach To Identify a Lead Scaffold That Targets the Translesion Synthesis Polymerase Rev1.J Chem Inf Model2018
30207151Conformational Dynamics of a Cysteine-Stabilized Plant Defensin Reveals an Evolutionary Mechanism to Expose Hydrophobic Residues.Biochemistry2018
30037752Small molecule scaffolds that disrupt the Rev1-CT/RIR protein-protein interaction.Bioorg Med Chem2018
30111544Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.Proc Natl Acad Sci U S A2018
28552172Protein folding by NMR.Prog Nucl Magn Reson Spectrosc2017
28401755Structural Characterization of the Early Events in the Nucleation-Condensation Mechanism in a Protein Folding Process.J Am Chem Soc2017
28265855NMR resonance assignments for the N-terminal domain of the δ subunit of the E. coli γ clamp loader complex.Biomol NMR Assign2017
28541665Identification of Small Molecule Translesion Synthesis Inhibitors That Target the Rev1-CT/RIR Protein-Protein Interaction.ACS Chem Biol2017
26982350Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Polζ Suggests a Mechanism of Polymerase Exchange upon Rev1/Polζ-Dependent Translesion Synthesis.Biochemistry2016
27771863Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins.J Biomol NMR2016
27362876Targeting the Translesion Synthesis Pathway for the Development of Anti-Cancer Chemotherapeutics.J Med Chem2016
26115097Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy.Biochemistry2015
26051180HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.Mol Cell2015
26224631Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.J Biol Chem2015
25162118NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.Biochemistry2014
23084974Loss of structure-gain of function.J Mol Biol2013
23907177PHD domain from human SHPRH.J Biomol NMR2013
23747975NMR mapping of PCNA interaction with translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain.J Mol Biol2013
22148426Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-Rosetta.J Phys Chem B2012
22955930In support of the BMRB.Nat Struct Mol Biol2012
22691049NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase η.Biochemistry2012
22828282The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζ.FEBS Lett2012
22647611Transiently populated intermediate functions as a branching point of the FF domain folding pathway.Proc Natl Acad Sci U S A2012
21639149Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.J Am Chem Soc2011
20033258Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods.J Biomol NMR2010
20829478A transient and low-populated protein-folding intermediate at atomic resolution.Science2010
20799727NMR characterization of copper-binding domains 4-6 of ATP7B .Biochemistry2010
20428928A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states.J Biomol NMR2010
19111555Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy.J Mol Biol2009
19569643An analysis of the effects of 1HN-(1)HN dipolar couplings on the measurement of amide bond vector orientations in invisible protein states by relaxation dispersion NMR.J Phys Chem B2009
18275162Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.Acc Chem Res2008
17306298Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study.J Mol Biol2007
17726107Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain.Proc Natl Acad Sci U S A2007
17689561The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy.J Mol Biol2007
16608362Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion.J Am Chem Soc2006
16922492Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.Biochemistry2006
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Collaborators

University of Toronto
Co-authored papers 29
University of Connecticut Health Center
Co-authored papers 18
University of Cambridge
Co-authored papers 4
Medical Research Council Laboratory of Molecular Biology
Co-authored papers 4
Hospital for Sick Children
Co-authored papers 3
University of Toronto, University Avenue
Co-authored papers 3
Dana-Farber Cancer Institute
Co-authored papers 2
University of Toronto
Co-authored papers 2
University of Connecticut School of Medicine
Co-authored papers 2
University of Connecticut Health Center
Co-authored papers 2
University of California San Francisco
Co-authored papers 1
Rutgers University
Co-authored papers 1
Center for Integrated Protein Science, Technische Universitat Munchen
Co-authored papers 1
Leicester Institute of Structural and Chemical Biology, University of Leicester
Co-authored papers 1
University of Texas Southwestern Medical Center
Co-authored papers 1
The University of Sheffield
Co-authored papers 1
Institute of Systems, The University of Liverpool
Co-authored papers 1
Institute of Integrative Biology, University of Liverpool
Co-authored papers 1
Columbia University
Co-authored papers 1
National Institutes of Health
Co-authored papers 1
Zernike Institute for Advanced Materials, University of Groningen
Co-authored papers 1
Co-authored papers 1
University of Oxford
Co-authored papers 1
The Medical Research Council Biomedical NMR Centre, The Francis Crick Institute
Co-authored papers 1
University of Cambridge
Co-authored papers 1
Carnegie Mellon University
Co-authored papers 1
Imperial College London
Co-authored papers 1
Carnegie Mellon University
Co-authored papers 1
Institute for Protein Research, Osaka University
Co-authored papers 1
Sichuan University
Co-authored papers 1